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Actin Filament Depolymerization01:19

Actin Filament Depolymerization

3.1K
Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
3.1K
Actin Polymerization01:42

Actin Polymerization

6.6K
Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶  nucleation, elongation, and steady-state phase.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight...
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Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
2.9K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.0K
The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
3.0K
Actin Treadmilling01:18

Actin Treadmilling

8.0K
Actin filaments undergo polymerization and depolymerization from either end. The polymerization and depolymerization rates depend on the cytosolic concentration of free G-actins. The polymerization rate is generally higher at the plus or barbed end, while the depolymerization rate is higher at the minus or pointed end. At a steady state, critical concentration describes the concentration of free G-actin monomers at which the polymerization rate at the plus end is equal to that of the...
8.0K
Introduction to Actin01:26

Introduction to Actin

5.2K
Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution.  Actin coding genes are conserved within species and across...
5.2K

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Related Experiment Video

Updated: Jul 2, 2025

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
08:02

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

Published on: May 5, 2022

2.6K

Depolymerization of actin filaments by Cucurbitacin I through binding G-actin.

Ebru Haciosmanoglu Aldogan1, Kemal Alper Önsü2, Cemil Can Saylan3

  • 1Department of Biophysics, Faculty of Medicine Bezmialem Vakif University Istanbul Turkey.

Food Science & Nutrition
|February 19, 2024
PubMed
Summary

Cucurbitacin I (CuI) directly binds G-actin, stabilizing it and inhibiting actin polymerization. This actin targeting reveals a novel mechanism for CuI

Keywords:
F‐actinG‐actinactin dynamicscell migrationcucurbitacin Itarget protein

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A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
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A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
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A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

Published on: June 3, 2021

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Pharmacology

Background:

  • Cucurbitacins possess significant economic and pharmacological value.
  • Cucurbitacin I (CuI) exhibits anticancer properties by inhibiting the JAK2-STAT3 pathway.
  • The actin cytoskeleton is crucial for cellular functions and is regulated by dynamic reorganization.

Purpose of the Study:

  • To investigate the direct impact of Cucurbitacin I (CuI) on actin dynamics.
  • To elucidate the molecular mechanisms underlying CuI's interaction with actin.
  • To explore CuI's potential as an actin-targeting anticancer agent.

Main Methods:

  • Thermal shift assays to assess G-actin-CuI binding.
  • In vitro actin polymerization assays.
  • Endothelial cell treatments to visualize actin filament disruption.
  • Molecular docking and molecular dynamics (MD) simulations.
  • Cell migration assays.

Main Results:

  • CuI binding to G-actin increased its thermal stability.
  • CuI dose-dependently inhibited F-actin polymerization in vitro.
  • CuI disrupted actin filaments in endothelial cells.
  • Molecular simulations identified a specific binding site for CuI on F-actin.
  • CuI treatment significantly reduced cell migration ability.

Conclusions:

  • CuI directly binds to G-actin, stabilizing it and affecting actin dynamics.
  • CuI inhibits actin polymerization and disrupts actin filaments, revealing a novel mechanism of action.
  • CuI's direct interaction with actin suggests its potential as an actin-targeting anticancer drug.